Crystal structure of Bacillus cereus HlyIIR, a transcriptional regulator of the gene for pore-forming toxin hemolysin II

Oleg V. Kovalevskiy; Andrey A. Lebedev; Alexei K. Surin; Alexander S. Solonin; Alfred A. Antson

doi:10.1016/j.jmb.2006.10.074

Crystal structure of Bacillus cereus HlyIIR, a transcriptional regulator of the gene for pore-forming toxin hemolysin II

Oleg V. Kovalevskiy, Andrey A. Lebedev, Alexei K. Surin, Alexander S. Solonin, Alfred A. Antson

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

Production of Bacillus cereus and Bacillus anthracis toxins is controlled by a number of transcriptional regulators. Here we report the crystal structure of B. cereus HlyIIR, a regulator of the gene encoding the pore-forming toxin hemolysin II. We show that HlyIIR forms a tight dimer with a fold and overall architecture similar to the TetR family of repressors. A remarkable feature of the structure is a large internal cavity with a volume of 550 angstrom(3) suggesting that the activity of HlyIIR is modulated by binding of a ligand, which triggers the toxin production. Virtual ligand library screening shows that this pocket can accommodate compounds with molecular masses of up to 400-500 Da. Based on structural data and previous biochemical evidence, we propose a model for HlyIIR interaction with the DNA. (c) 2006 Elsevier Ltd. All rights reserved.

Original language	English
Pages (from-to)	825-834
Number of pages	10
Journal	Journal of Molecular Biology
Volume	365
Issue number	3
DOIs	https://doi.org/10.1016/j.jmb.2006.10.074
Publication status	Published - 19 Jan 2007

Keywords

HlyIIR
X-ray crystallography
DNA-binding
TetR family
hemolysin II
MOLECULAR-GRAPHICS
BINDING PROTEIN
TET REPRESSOR
DNA-BINDING
SEQUENCE
RESISTANCE
REFINEMENT
VIRULENCE
ANTHRACIS
RECEPTOR

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10.1016/j.jmb.2006.10.074

Cite this

@article{3603963564df4496b513e5c5b39ca499,

title = "Crystal structure of Bacillus cereus HlyIIR, a transcriptional regulator of the gene for pore-forming toxin hemolysin II",

abstract = "Production of Bacillus cereus and Bacillus anthracis toxins is controlled by a number of transcriptional regulators. Here we report the crystal structure of B. cereus HlyIIR, a regulator of the gene encoding the pore-forming toxin hemolysin II. We show that HlyIIR forms a tight dimer with a fold and overall architecture similar to the TetR family of repressors. A remarkable feature of the structure is a large internal cavity with a volume of 550 angstrom(3) suggesting that the activity of HlyIIR is modulated by binding of a ligand, which triggers the toxin production. Virtual ligand library screening shows that this pocket can accommodate compounds with molecular masses of up to 400-500 Da. Based on structural data and previous biochemical evidence, we propose a model for HlyIIR interaction with the DNA. (c) 2006 Elsevier Ltd. All rights reserved.",

keywords = "HlyIIR, X-ray crystallography, DNA-binding, TetR family, hemolysin II, MOLECULAR-GRAPHICS, BINDING PROTEIN, TET REPRESSOR, DNA-BINDING, SEQUENCE, RESISTANCE, REFINEMENT, VIRULENCE, ANTHRACIS, RECEPTOR",

author = "Kovalevskiy, {Oleg V.} and Lebedev, {Andrey A.} and Surin, {Alexei K.} and Solonin, {Alexander S.} and Antson, {Alfred A.}",

year = "2007",

month = jan,

day = "19",

doi = "10.1016/j.jmb.2006.10.074",

language = "English",

volume = "365",

pages = "825--834",

journal = "Journal of Molecular Biology",

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TY - JOUR

T1 - Crystal structure of Bacillus cereus HlyIIR, a transcriptional regulator of the gene for pore-forming toxin hemolysin II

AU - Kovalevskiy, Oleg V.

AU - Lebedev, Andrey A.

AU - Surin, Alexei K.

AU - Solonin, Alexander S.

AU - Antson, Alfred A.

PY - 2007/1/19

Y1 - 2007/1/19

N2 - Production of Bacillus cereus and Bacillus anthracis toxins is controlled by a number of transcriptional regulators. Here we report the crystal structure of B. cereus HlyIIR, a regulator of the gene encoding the pore-forming toxin hemolysin II. We show that HlyIIR forms a tight dimer with a fold and overall architecture similar to the TetR family of repressors. A remarkable feature of the structure is a large internal cavity with a volume of 550 angstrom(3) suggesting that the activity of HlyIIR is modulated by binding of a ligand, which triggers the toxin production. Virtual ligand library screening shows that this pocket can accommodate compounds with molecular masses of up to 400-500 Da. Based on structural data and previous biochemical evidence, we propose a model for HlyIIR interaction with the DNA. (c) 2006 Elsevier Ltd. All rights reserved.

AB - Production of Bacillus cereus and Bacillus anthracis toxins is controlled by a number of transcriptional regulators. Here we report the crystal structure of B. cereus HlyIIR, a regulator of the gene encoding the pore-forming toxin hemolysin II. We show that HlyIIR forms a tight dimer with a fold and overall architecture similar to the TetR family of repressors. A remarkable feature of the structure is a large internal cavity with a volume of 550 angstrom(3) suggesting that the activity of HlyIIR is modulated by binding of a ligand, which triggers the toxin production. Virtual ligand library screening shows that this pocket can accommodate compounds with molecular masses of up to 400-500 Da. Based on structural data and previous biochemical evidence, we propose a model for HlyIIR interaction with the DNA. (c) 2006 Elsevier Ltd. All rights reserved.

KW - HlyIIR

KW - X-ray crystallography

KW - DNA-binding

KW - TetR family

KW - hemolysin II

KW - MOLECULAR-GRAPHICS

KW - BINDING PROTEIN

KW - TET REPRESSOR

KW - DNA-BINDING

KW - SEQUENCE

KW - RESISTANCE

KW - REFINEMENT

KW - VIRULENCE

KW - ANTHRACIS

KW - RECEPTOR

U2 - 10.1016/j.jmb.2006.10.074

DO - 10.1016/j.jmb.2006.10.074

M3 - Article

SN - 0022-2836

VL - 365

SP - 825

EP - 834

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 3

ER -